Reviewed, UniProtKB/Swiss-Prot P17066 (HSP76_HUMAN)

Names and origin

Protein names

Recommended name:
    Heat shock 70 kDa protein 6
Alternative name(s):
    Heat shock 70 kDa protein B'

Gene names

Name:	HSPA6
Synonyms:	HSP70B'

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	643 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage By similarity.
Induction	Only at higher temperatures, and no basal expression.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	response to unfolded protein Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 643

643

Heat shock 70 kDa protein 6

PRO_0000078264

Amino acid modifications

Modified residue

321

1

N6-acetyllysine Ref.8

Modified residue

502

1

N6-acetyllysine Ref.8

Natural variations

Natural variant

65

1

P → T

VAR_060718

Natural variant

95

1

R → Q

VAR_060719

Natural variant

150

1

A → T: dbSNP rs10919224. Ref.2

VAR_049605

Natural variant

153

1

N → S: dbSNP rs10919225. Ref.2

VAR_049606

Natural variant

154

1

D → N: dbSNP rs10919226. Ref.2

VAR_049607

Natural variant

159

1

A → V

VAR_060720

Natural variant

170

1

N → K: dbSNP rs41297704. Ref.2

VAR_049608

Natural variant

173

1

R → P: dbSNP rs41297708. Ref.2

VAR_049609

Natural variant

178

1

P → A: dbSNP rs41297710. Ref.2

VAR_049610

Natural variant

194

1

E → K: dbSNP rs41297714. Ref.2

VAR_049611

Natural variant

198

1

L → F: dbSNP rs1079109. Ref.2

VAR_024182

Natural variant

260

1

R → H: dbSNP rs41299256.

VAR_049612

Natural variant

297

1

T → K

VAR_060721

Natural variant

336

1

V → F: dbSNP rs417707.

VAR_059360

Natural variant

464

1

S → I: dbSNP rs388218. Ref.2

VAR_049613

Natural variant

471

1

R → H: dbSNP rs41299256. Ref.2

VAR_049614

Natural variant

528

1

K → E: dbSNP rs570189. Ref.2

VAR_049615

Natural variant

528

1

K → R: dbSNP rs570167.

VAR_059361

Natural variant

562

1

D → E: dbSNP rs753856. Ref.2

VAR_024183

Natural variant

572

1

M → V: dbSNP rs452004.

VAR_049616

Natural variant

577

1

R → Q: dbSNP rs368844. Ref.2

VAR_049617

Natural variant

626

1

T → A: dbSNP rs41299260. Ref.2

VAR_049618

Experimental info

Sequence conflict

106 – 108

3

RVC → PVS Ref.1

Sequence conflict

106 – 108

3

RVC → PVS Ref.3

Sequence conflict

263

1

R → G in CAA36061. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

643

Helix Strand Turn

Details...

Beta strand

17 – 19

3

Beta strand

39 – 41

3

Beta strand

44 – 46

3

Helix

56 – 59

4

Turn

60 – 63

4

Helix

65 – 67

3

Helix

72 – 74

3

Helix

83 – 90

8

Beta strand

93 – 98

6

Beta strand

103 – 108

6

Beta strand

113 – 116

4

Helix

118 – 136

19

Beta strand

143 – 148

6

Helix

154 – 162

9

Beta strand

170 – 176

7

Helix

177 – 184

8

Beta strand

195 – 202

8

Beta strand

208 – 214

7

Beta strand

219 – 225

7

Helix

234 – 250

17

Helix

259 – 275

17

Turn

276 – 278

3

Beta strand

280 – 286

7

Beta strand

295 – 300

6

Helix

301 – 314

14

Helix

316 – 326

11

Helix

330 – 332

3

Beta strand

334 – 339

6

Helix

346 – 355

10

Turn

367 – 372

6

Helix

376 – 382

7

Sequences

	Sequence		Length	Mass (Da)
	P17066-1 [UniParc]. Last modified September 19, 2003. Version 2. Checksum: BCE348F0226DB70B	FASTA	643	71,028
	10 20 30 40 50 60 MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ 70 80 90 100 110 120 AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG GKPKVRVCYR GEDKTFYPEE 130 140 150 160 170 180 ISSMVLSKMK ETAEAYLGQP VKHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA 190 200 210 220 230 240 AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV 250 260 270 280 290 300 NHFMEEFRRK HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT 310 320 330 340 350 360 RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK LLQDFFNGKE 370 380 390 400 410 420 LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA 430 440 450 460 470 480 TIPTKQTQTF TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF 490 500 510 520 530 540 DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA 550 560 570 580 590 600 KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE 610 620 630 640 LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA." Leung T.K.C., Rajendran M.Y., Monfries C., Hall C., Lim L. Biochem. J. 267:125-132(1990) [PubMed: 2327978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Lung.
[2]	NIEHS SNPs program Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-65; GLN-95; THR-150; SER-153; ASN-154; VAL-159; LYS-170; PRO-173; ALA-178; LYS-194; PHE-198; LYS-297; ILE-464; HIS-471; GLU-528; GLU-562; GLN-577 AND ALA-626.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary and Skin.
[5]	"The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1." Leung T.K.C., Hall C., Rajendran M., Spurr N.K., Lim L. Genomics 12:74-79(1992) [PubMed: 1346391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-250.
[6]	"Cis-acting elements involved in the regulated expression of a human HSP70 gene." Schiller P., Amin J., Ananthan J., Brown M.E., Scott W.A., Voellmy R. J. Mol. Biol. 203:97-105(1988) [PubMed: 3184191] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321 AND LYS-502, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X51757 Genomic DNA. Translation: CAA36061.1.
X51758 mRNA. Translation: CAA36062.1.
DQ521571 Genomic DNA. Translation: ABF47108.1.
AL590385 Genomic DNA. Translation: CAI16120.1.
BC004279 mRNA. Translation: AAH04279.1.
BC035665 mRNA. Translation: AAH35665.1.
S78631 Genomic DNA. No translation available.

IPI

IPI00339269.

PIR

S09036.

RefSeq

NP_002146.2.

UniGene

Hs.654614

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FE1	X-ray	2.20	A/B/C	6-385	[»]

SMR

P17066. Positions 8-549, 396-617.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17066. 13 interactions.

STRING

P17066.

PTM databases

PhosphoSite

P17066.

2-D gel databases

HSC-2DPAGE

P17066.

Proteomic databases

PRIDE

P17066.

Genome annotation databases

Ensembl

ENST00000309758; ENSP00000310219; ENSG00000173110; Homo sapiens. [Genome view]

GeneID

3310.

KEGG

hsa:3310.

UCSC

uc001gap.1. human.

Organism-specific databases

CTD

3310.

GeneCards

GC01P159760.
GC01P159761.

HGNC

HGNC:5239. HSPA6.

HPA

CAB017452.

MIM

140555. gene.

PharmGKB

PA29505.

GenAtlas

Search...

Phylogenomic databases

eggNOG

maNOG16200.

HOGENOM

HBG334976.

HOVERGEN

P17066.

InParanoid

P17066.

OMA

QAAVLMG.

OrthoDB

EOG9TQPV5.

PhylomeDB

P17066.

Gene expression databases

ArrayExpress

P17066.

Bgee

P17066.

CleanEx

HS_HSPA6.

Genevestigator

P17066.

GermOnline

ENSG00000173110. Homo sapiens.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]

PANTHER

PTHR19375. Hsp70. 1 hit.

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

13127.

SOURCE

Search...

Entry information

Entry name

HSP76_HUMAN

Accession

Primary (citable) accession number: P17066
Secondary accession number(s): Q1HBA8, Q8IYK7, Q9BT95

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	September 19, 2003
Last modified:	January 19, 2010
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.